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See detailGalectin-1 accumulation in the ovary carcinoma peritumoral stroma is induced by ovary carcinoma cells and affects both cancer cell proliferation and adhesion to laminin-1 and fibronectin
van den Brule, Frédéric; Califice, Stéphane; Garnier, Frédérique et al

in Laboratory Investigation : Journal of Technical Methods & Pathology (2003), 83(3), 377-386

Galectin-1 (gal-1) is a 14-kDa laminin-binding galectin involved in several biologic events including regulation of cancer cell proliferation and adhesion to the matrix. In this study, we examined gal-1 ... [more ▼]

Galectin-1 (gal-1) is a 14-kDa laminin-binding galectin involved in several biologic events including regulation of cancer cell proliferation and adhesion to the matrix. In this study, we examined gal-1 expression in 30 human epithelial ovary carcinoma samples by Western and Northern blotting and by immunohistochemistry. Gal-1 mRNA levels were increased in more than 95% of the examined ovary carcinoma samples, compared with a wedge resection of a normal ovary. Immunohistochemical analysis of the samples demonstrated gal-1 expression in cancer epithelial cells from 17 of 30 samples, with a cytoplasmic pattern. Gal-1 immunostaining was significantly increased in the stroma associated with carcinoma cells compared with the normal, noninvaded stroma (p = 0.003). This pattern of expression was confirmed by examination of 12 other frozen epithelial ovary carcinomas, using in situ hybridization. Immunohistochemical staining of the specimens demonstrated colocalization of gal-1, laminin-1, and fibronectin. In vitro experiments were conducted to elucidate the potential biologic role of gal-1 in ovarian cancer progression. Gal-1 protein expression and release was detected in AZ364, SK-OV-3, and AZ224, but not in OVCAR-3, AZ419, and AZ382, human ovary carcinoma cell lines. Incubation of 84BR fibroblasts with conditioned media harvested from the ovary carcinoma cell lines induced an increased expression of gal-1 in the cultured fibroblasts in all cases except AZ419 and SK-OV-3. High concentrations of gal-1 (100 mug/ml) induced significantly decreased cell proliferation in all cell lines, as defined by bromodeoxyuridine incorporation. Additionally, recombinant gal-1 induced a dose-dependent increase in in vitro adhesion of AZ224, SK-OV-3, and AZ382 cells to laminin-1; adhesion to fibronectin was increased by gal-1 in OVCAR-3, AZ224, and SK-OV-3. No effect was observed in the other cases. Our data contribute to define a role for gal-1 during the interactions between human ovary carcinoma cells and host fibroblasts. [less ▲]

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See detailGalectin-1 Expression in Prostate Tumor-Associated Capillary Endothelial Cells Is Increased by Prostate Carcinoma Cells and Modulates Heterotypic Cell-Cell Adhesion
Clausse, Nathalie; van den Brule, Frédéric; Waltregny, David ULg et al

in Angiogenesis (1999), 3(4), 317-25

Besides providing tumors with nutrients, newly formed capillaries constitute a potential escape route for tumor cells favoring metastatic dissemination, and constitute an access for the anti-tumoral host ... [more ▼]

Besides providing tumors with nutrients, newly formed capillaries constitute a potential escape route for tumor cells favoring metastatic dissemination, and constitute an access for the anti-tumoral host immune cells. Galectin-1, a soluble human lectin, is involved in numerous biological functions including cell-cell and cell-substrate interactions. In addition, galectin-1 is able to induce apoptosis of activated T-lymphocytes. In this study, we have examined galectin-1 expression in capillaries associated to the carcinoma cells or present in the remote non-tumoral stroma of 100 human prostate carcinoma samples by immunoperoxidase staining. Galectin-1 was expressed by endothelial cells from capillaries infiltrating the tumor tissue in 64% (64/100) of the cases. On the contrary, endothelial cells in the adjacent non-tumoral stroma expressed galectin-1 in very few cases (7/100). Increased frequency of galectin-1-positive capillaries in the tumor-associated compared to the tumor-free areas was observed in 63% of the cases. This striking contrast led us to set up an in vitro model to test whether tumor cells could induce galectin-1 expression by endothelial cells. Incubation of human umbilical vein endothelial cells with conditioned media from PC-3 or DU 145 prostate carcinoma cells led to a significant increase of galectin-1 protein expression (+32.97% and 37.91% P < 0.01 and P < 0.05, respectively). PC-3 conditioned medium also induced increased adhesion values of PC-3 cells to the endothelial cells (53.4 +/- 4.7 vs. 38.5 +/- 3.5 after 30 min; 66.6 +/- 7.8 vs. 46.2 +/- 6.4 after 60 min). An anti-galectin-1 antiserum abolished this modulation, and recombinant galectin-1 also induced increased adhesion values in a dose-dependent fashion. This effect was specific as no such modulations were observed using normal lymphocytes instead of PC-3 cells. Preferential galectin-1 expression in the endothelial cells close to the cancer cells could provide these latter with increased abilities to interact with the endothelial cells as well as a defense against the host immune system. [less ▲]

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See detailGalectin-1 in Melanoma Biology and Related Neo-Angiogenesis Processes.
Mathieu, V.; de Lassalle, Elisabeth Martin; Toelen, J. et al

in Journal of Investigative Dermatology (2012)

Aggressiveness of advanced melanomas relates in part to their marked propensity to develop neoangiogenesis and metastases. Among its numerous pro-cancer roles, galectin (gal)-1 expressed and/or secreted ... [more ▼]

Aggressiveness of advanced melanomas relates in part to their marked propensity to develop neoangiogenesis and metastases. Among its numerous pro-cancer roles, galectin (gal)-1 expressed and/or secreted by both cancer and endothelial cells stimulates proliferation and angiogenesis. This study first shows that gal-1 is more highly expressed at both mRNA and protein levels than its congeners in melanomas and particularly in advanced lesions. The roles of gal-1 were further investigated in vivo in the highly proliferating and vascularized pseudometastatic B16F10 mouse melanoma model using stable knockdown B16F10 cells and wild-type versus gal-1 knockout mice, and then in vitro in B16F10 tumoral and lung microvascular cells. Gal-1 depletion in the B16F10 tumor cells but not in the tumor-bearing mice significantly increased melanoma-bearing mice survival. Tumor-derived gal-1 thus seems to have more critical roles than the host-derived one. In fact, gal-1 displays distinct effects on the H-Ras-dependent p53/p21 pathways: in primary lung microvessel endothelial cells, gal-1 seems to be involved in the maintenance of senescent status through the induction of both p53 and p21 while it stimulates B16F10 cancer cell proliferation through a p53/p21 decrease. Altogether, these data point to gal-1 as a potential target to combat melanomas.Journal of Investigative Dermatology advance online publication, 24 May 2012; doi:10.1038/jid.2012.142. [less ▲]

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See detailGalectin-1 Modulates Human Melanoma Cell Adhesion to Laminin
van den Brule, F. A.; Buicu, C.; Baldet, M. et al

in Biochemical and Biophysical Research Communications (1995), 209(2), 760-7

Galectins constitute a gene family of beta-galactoside-specific lectins that show high homology in their carbohydrate-binding site. They have been postulated to be involved in many biological events, but ... [more ▼]

Galectins constitute a gene family of beta-galactoside-specific lectins that show high homology in their carbohydrate-binding site. They have been postulated to be involved in many biological events, but their specific functions are not yet well defined. Galectin-1 is a laminin binding protein that recognizes poly-N-acetyllactosamine chains on this major basement membrane glycoprotein. In this study, we analyzed the possibility that galectin-1 could modulate interactions between human melanoma cells and laminin. We demonstrated that A375 and A2058 cell lines express galectin-1 both intracellularly and on the cell surface. In an in vitro assay, recombinant galectin-1 increased melanoma cell attachment to laminin in a dose-dependent manner. This effect was abolished by lactose. Anti-galectin-1 inhibited adhesion of melanoma cells to laminin in a dose-dependent fashion. However, neither galectin-1 nor anti-galectin-1 antibody affected melanoma cell spreading on laminin in vitro. These data indicate that galectin-1 might participate in melanoma cell adhesion to laminin and therefore could be a modulator of invasion and metastasis. [less ▲]

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See detailGalectin-3 and Cancer (Review)
Califice, Stéphane; Castronovo, Vincenzo ULg; van den Brûle, Fréderic

in International Journal of Oncology (2004), 25(4), 983-92

Galectin-3 is a pleiotropic carbohydrate-binding protein involved in a variety of normal and pathological biological processes. Its carbohydrate-binding properties constitute the basis for cell-cell and ... [more ▼]

Galectin-3 is a pleiotropic carbohydrate-binding protein involved in a variety of normal and pathological biological processes. Its carbohydrate-binding properties constitute the basis for cell-cell and cell-matrix interactions and cancer progression. Modulation of galectin-3 expression in cancer cells has indeed been reported. These observations lead to the recognition of galectin-3 as a diagnostic/prognostic marker for specific cancer types, such as thyroid and prostate. This review discusses the expression and cellular localization of galectin-3 in cancer cells, as well as its numerous functions in cancer cell biology, including cell-cell adhesion, cell-matrix interactions, growth regulation, apoptosis, angiogenesis and mRNA splicing. [less ▲]

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See detailGalectin-3 and laminin expression in neoplastic and non-neoplastic thyroid tissue.
Fernandez, P. L.; Merino, M. J.; Gomez, M. et al

in Journal of Pathology (The) (1997), 181(1), 80-6

Galectin-3 is a 31 kD beta-galactoside-binding lectin which is expressed by several types of non-neoplastic and neoplastic cells and which may be involved in cell-extracellular matrix interactions. An ... [more ▼]

Galectin-3 is a 31 kD beta-galactoside-binding lectin which is expressed by several types of non-neoplastic and neoplastic cells and which may be involved in cell-extracellular matrix interactions. An immunohistochemical study has been made of the expression of galectin-3, as well as its ligand, laminin, in a spectrum of benign and malignant thyroid neoplasms and in some non-neoplastic conditions. Immunohistochemistry with anti-human recombinant galectin-3 antibody showed consistent, intense positivity in the neoplastic cells of 18 cases of papillary carcinoma and less intense staining in the five anaplastic carcinomas studied. In addition, two out of three poorly differentiated carcinomas, three out of six medullary carcinomas, and four out of eight follicular carcinomas had less intense or focal positivity. One case of Hurthle cell carcinoma showed scattered strongly positive cells. Eight follicular adenomas, three hyperplastic nodules, five nodular goitres, and normal thyroid tissue were negative. Galectin-3 mRNA expression was also evaluated in three of the papillary carcinomas, two follicular adenomas, and one hyperplastic nodule with matched normal tissue. Northern blot analysis demonstrated mRNA overexpression in the three cases of papillary carcinomas, whereas normal and benign tissues were negative. Laminin distribution in neoplastic and non-neoplastic tissue varied with architectural patterns but did not correlate with galectin-3 immunohistochemical expression. We conclude that expression of galectin-3 is limited to inflammatory foci in normal and benign thyroid tissue and is a phenotypic feature of malignant thyroid neoplasms, especially papillary carcinomas. [less ▲]

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See detailGalectin-3, a Laminin Binding Protein, Fails to Modulate Adhesion of Human Melanoma Cells to Laminin
van den Brule, F. A.; Buicu, C.; Sobel, M. E. et al

in Neoplasma (1995), 42(5), 215-9

Galectin-3 is a laminin binding protein which expression is altered in a variety of human carcinomas including colon, breast and endometrium. In these tumors, we consistently observed a down regulation of ... [more ▼]

Galectin-3 is a laminin binding protein which expression is altered in a variety of human carcinomas including colon, breast and endometrium. In these tumors, we consistently observed a down regulation of galectin-3 expression related to increased aggressiveness. Galectin-3 belongs to a family of galactose-binding lectins and binds laminin through its numerous poly-N-acetyllactosamine chains. To date, the exact role of galectin-3 in the complex interactions between cancer cells and laminin has not been clearly defined. Adhesion of melanoma cells to laminin is a critical event during tumor invasion and metastasis. In this study, we explore the possibility that galectin-3 could modulate attachment of two human melanoma cell lines to laminin. A2058 and A375 melanoma cell expressed galectin-3 on their surface as demonstrated by immunofluorescence, and attached to laminin in an in vitro assay. We demonstrate that neither recombinant galectin-3 nor an affinity purified antigalectin-3 antiserum altered adhesion of A2058 or A375 melanoma cells to laminin. Our data strongly suggest that galectin-3 is not a key element in adhesion of the melanoma cells to laminin. These results are not surprising in light of the observation that galectin-3 expression is down regulated in cancer and that increased adhesion to laminin is a constant feature of invasive cancer cells. [less ▲]

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See detailGalectin-3: a new promising cardiac biomarker in sports endurance?
LE GOFF, Caroline ULg; Devaux, Séverine; BREVERS, Eric ULg et al

in Cardiovascular Research (2014, July), 103(Supplement 1),

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See detailGalectin-9 in tumor biology: a jack of multiple trades
Heusschen, Roy ULg; Griffioen, Arjan; Thijssen, Victor

in Biochimica et Biophysica Acta - Reviews on Cancer (2013)

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See detailGalectins: a family of animal beta-galactoside-binding lectins.
Barondes, S. H.; Castronovo, Vincenzo ULg; Cooper, D. N. et al

in Cell (1994), 76(4), 597-8

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See detailGalerkin and de Rham Discretizations for Hybrid Methods
Geuzaine, Christophe ULg; Tarhasaari, T.; Kettunen, L. et al

in Proceedings of the 9th IEEE Conference on Electromagnetic Field Computation (CEFC'2000) (2000)

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See detailA Galerkin projection method for mixed finite elements
Geuzaine, Christophe ULg; Meys, B.; Dular, Patrick ULg et al

in IEEE Transactions on Magnetics (1999), 35(3), 1438--1441

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See detailA Galerkin projection method for mixed finite elements
Geuzaine, Christophe ULg; Meys, B.; Dular, Patrick ULg et al

in Proceedings of the Eighth Biennal IEEE Conference on Electromagnetic Field Computation (1998)

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See detailGalilée et la naissance de la science moderne
De Rop, Yves ULg

Article for general public (1992)

Not Available

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See detailGalileo : une boussole spatiale européenne réglée par des ingénieurs belges
Bidaine, Benoît ULg

in Journal des Ingénieurs (Le) (2009), (121), 9-11

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See detailGalileo ? Bien plus qu’un système de positionnement !
Warnant, René ULg

Conference given outside the academic context (2010)

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See detailGalileo Local Component for the detection of atmospheric threats
Warnant, René ULg; Bavier, Michaël; Brenot, Hugues et al

in Goodman, John (Ed.) Proceedings of the 12th International Ionospheric Effects Symposium (IES2008) (2008, May)

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See detailGalileo Local Component for the detection of atmospheric threats
Warnant, René ULg; Wautelet, Gilles ULg; Lejeune, Sandrine et al

Conference (2008, November)

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See detailGalileo Single Frequency Ionospheric Correction: Performances in Terms of Position
Bidaine, Benoît ULg; Lonchay, Matthieu ULg; Warnant, René ULg

in GPS Solutions (2013), 17(1), 63-73

For GPS single frequency users, the ionospheric contribution to the error budget is estimated by the well-known Klobuchar algorithm. For Galileo, it will be mitigated by a global algorithm based on the ... [more ▼]

For GPS single frequency users, the ionospheric contribution to the error budget is estimated by the well-known Klobuchar algorithm. For Galileo, it will be mitigated by a global algorithm based on the NeQuick model. This algorithm relies on the adaptation of the model to slant Total Electron Content (sTEC) measurements. Although the performance specifications of these algorithms are expressed in terms of delay and TEC, the users might be more interested in their impact on positioning. Therefore, we assessed the ability of the algorithms to improve the positioning accuracy using globally distributed permanent stations for the year 2002 marked by a high level of solar activity. We present uncorrected and corrected performances, interpret these and identify potential causes for Galileo correction discrepancies. We show vertical errors dropping by 56–64 % due to the analyzed ionospheric corrections, but horizontal errors decreasing by 27 % at most. By means of a fictitious symmetric satellite distribution, we highlight the role of TEC gradients in residual errors. We describe mechanisms permitted by the Galileo correction, which combine sTEC adaptation and topside mismodeling, and limit the horizontal accuracy. Hence, we support further investigation of potential alternative ionospheric corrections. We also provide an interesting insight into the ionospheric effects possibly experienced during the next solar maximum coinciding with Galileo Initial Operation Capability. [less ▲]

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See detailGalileo Single Frequency Ionospheric Correction: Performances in Terms of Position
Bidaine, Benoît ULg; Warnant, René ULg

in Goodman, John M. (Ed.) 2011 Ionospheric Effects Symposium Proceedings (2011, May)

The ionospheric effect remains one of the main factors limiting GNSS accuracy. For GPS single frequency users, this contribution to the error budget is estimated thanks to the well-known Klobuchar ... [more ▼]

The ionospheric effect remains one of the main factors limiting GNSS accuracy. For GPS single frequency users, this contribution to the error budget is estimated thanks to the well-known Klobuchar algorithm. For Galileo, it will be mitigated by a global algorithm based on the NeQuick model. This algorithm relies on an optimisation procedure called ingestion. In this framework, an "effective ionisation level" Az plays the role of the solar activity information provided to the model in order to fit a specific dataset. For Galileo single frequency operation, daily Az values will be computed from slant Total Electron Content (sTEC) measurements performed within the ground segment and three coefficients will be broadcast to the users within the navigation message allowing them to run the model. The performance specifications of these algorithms are respectively expressed in terms of delay and TEC but the users might find more interest in their impact on positioning. Hence we propose to investigate their performances in terms of positioning accuracy. To this extent we compare positions of permanent stations calculated with and without the ionospheric correction to the actual ones which are known at the sub-centimetre level. Our simulation uses sTEC generated from Global Ionospheric Maps to provide the effective ionization level coefficients and GPS single frequency code measurements to compute positions. We present results for Brussels station in Belgium (mid-latitudes) and for 2002 (high solar activity level). It gives an interesting insight in the situation we could observe when Galileo reaches its Initial Operation Capability, during the next solar maximum. This study constitutes a first step in the development of a real-time service in the framework of the SWANS project of the University of Liège and the Royal Meteorological Institute of Belgium. As two Galileo receivers have been bought in this context, this service will be available for the In-Orbit Validation phase of Galileo. [less ▲]

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